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KentuckyFC writes "X-ray crystallography has been a workhorse for chemists since the 1940s and 50s, revealing the 3D structure of complex biological molecules such as haemoglobin, DNA and insulin. But the technique has a severe limitation: it only works with molecules that form into crystals and that turns out to be a tiny fraction of the proteins that make up living things. But today, a team of US researchers say they have created the first image of a single uncrystallized virus using x-ray diffraction. The trick is to take a diffraction pattern of the virus and then subtract the diffraction pattern of its surroundings (abstract). The breakthrough paves the way for scientists to start teasing apart the 3D structures of the many proteins that have eluded biologists to date."

The reason X-ray diffraction needed a regular crystal not because it was impossible to get information but because there are limits on sensitivity and computation.

The first protein that X-ray crystallography was successfully used on was myoglobin. The processing included housewives recording the position of small,medium and large dots.

Now the sensitivity is much higher and the processing ability is astounding. This article is saying that they have figured out how to isolate the x-ray signal from a single protein. There is no reason that you can't get a high enough resolution to see the domains of a protein which often do have a regular crystal structure even if the whole protein doesn't.